Immunochemical and biochemical study of an abnormal heavy chain of bovine IgG1.
An abnormal heavy chain (HC) protein of IgG1 was isolated from the serum of a leukemic cow by gel filtration on a Sephadex G-200 column with the following ion-exchange chromatography. The HC protein migrated electrophoretically in the anodic region. The molecular weight of the untreated HC protein was about 48,000. Enzymatic treatment with papain and reduction with beta-mercaptoethanol showed no effect on the protein. Antigenic analysis of the HC protein using a specific rabbit antiserum against bovine IgG1 showed a complete identity with the Fc fragment and a partial identity with the intact bovine IgG1. Antigenic determinants of the light-chain were not found. The HC protein consisted of only one polypeptide chain.
D000818:Animals; D002417:Cattle; D002418:Cattle Diseases / Q000276:immunology*; D007120:Immunochemistry; D007074:Immunoglobulin G; D007143:Immunoglobulin Heavy Chains; D007945:Leukemia, Lymphoid / Q000276:immunology / Q000662:veterinary*; D008970:Molecular Weight
D007074:Immunoglobulin G; D007143:Immunoglobulin Heavy Chains